ArticleJournal of molecular biology2009
Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Structural analysis of YcdY, a member of the redox-enzyme maturation protein family.Acta crystallographica. Section F, Structural biology communications · 2025Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries.Heliyon · 2019Article
- Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.Microbiology (Reading, England) · 2016Article
- NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations.BMC evolutionary biology · 2015Article
- Biosynthesis and Insertion of the Molybdenum Cofactor.EcoSal Plus · 2015Review
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
- Unique Photobleaching Phenomena of the Twin-Arginine Translocase Respiratory Enzyme Chaperone DmsD.The open biochemistry journal · 2014Article
- The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.Biochemistry · 2013Article
- Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.The Biochemical journal · 2013Article
- Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.Molecular microbiology · 2012Article
- Conserved signal peptide recognition systems across the prokaryotic domains.Biochemistry · 2012Article
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
- The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.PloS one · 2012Article
- Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion.The Journal of biological chemistry · 2011Article
- Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates.FEBS letters · 2010Article
- Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The redox enzyme maturation proteins play an essential role in the proofreading and membrane targeting of protein substrates to the twin-arginine translocase. Functionally, the most thoroughly characterized redox enzyme maturation protein to date is Escherichia coli DmsD (EcDmsD). Herein, we present the X-ray crystal structure of the monomeric form of the EcDmsD refined to 2.0 A resolution, with clear electron density present for each of its 204 amino acid residues. The structural data presented here complement the biochemical data previously generated regarding the function of these twin-arginine translocase leader peptide binding chaperone proteins. Docking and molecular dynamics simulation experiments were used to provide a proposed model for how this chaperone is able to recognize the leader peptide of its substrate DmsA. The interactions observed in the model are in agreement with previous biochemical data and suggest intimate interactions between the conserved twin-arginine motif of the leader peptide of E. coli DmsA and the most conserved regions on the surface of EcDmsD.
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